|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-237 |
6.45e-81 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 244.97 E-value: 6.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 160 TEVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATI 208
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYvflfieamadagvalglpretarelaaqtvlGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 533112486 209 HALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-237 |
3.66e-75 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 230.61 E-value: 3.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIH 209
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYiflaiealadggvaaglprdvalslaaqtvlGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 533112486 210 ALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
47-236 |
5.97e-62 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 195.94 E-value: 5.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY-------------------------- 180
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYvflfiealadagvkqglprelalela 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533112486 181 -----GAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 236
Cdd:TIGR00112 185 aqtvkGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-236 |
2.78e-28 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 104.40 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 164 EDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 212
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYvflfiealadagvamglpreearelaaqtvlGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 533112486 213 VLESGGFRSLLINAVEASCIRTRE 236
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-237 |
6.45e-81 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 244.97 E-value: 6.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 160 TEVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATI 208
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYvflfieamadagvalglpretarelaaqtvlGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 533112486 209 HALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-237 |
3.66e-75 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 230.61 E-value: 3.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIH 209
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYiflaiealadggvaaglprdvalslaaqtvlGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 533112486 210 ALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-237 |
5.61e-68 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 211.93 E-value: 5.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADIEDrhIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK11880 81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVE-EDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATI 208
Cdd:PRK11880 156 WVDdEKQMDAVTAVSGSGPAYvflfiealadagvklglpreqarklaaqtvlGAAKLLLESGEHPAELRDNVTSPGGTTI 235
|
250 260
....*....|....*....|....*....
gi 533112486 209 HALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:PRK11880 236 AALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
47-236 |
5.97e-62 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 195.94 E-value: 5.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY-------------------------- 180
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYvflfiealadagvkqglprelalela 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533112486 181 -----GAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 236
Cdd:TIGR00112 185 aqtvkGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
1-243 |
1.11e-39 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 139.52 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07679 84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIH 209
Cdd:PRK07679 161 VVEEEDMHAVTALSGSGPAYiyyvveamekaakkiglkedvakslilqtmiGAAEMLKASEKHPSILRKEITSPGGTTEA 240
|
250 260 270
....*....|....*....|....*....|....
gi 533112486 210 ALHVLESGGFRSLLINAVEASCIRTRELQSMADQ 243
Cdd:PRK07679 241 GIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
1-237 |
5.45e-34 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 124.29 E-value: 5.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKmgvkltphNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PTZ00431 4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKVLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIgADIEDRHIVVSCAAGVTISSIEKKLSAfrpAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PTZ00431 76 EI-KPYLGSKLLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVEEDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIH 209
Cdd:PTZ00431 152 EIKEKDMDIATAISGCGPAYvflfieslidagvknglnrdvsknlvlqtilGSVHMVKASDQPVQQLKDDVCSPGGITIV 231
|
250 260
....*....|....*....|....*...
gi 533112486 210 ALHVLESGGFRSLLINAVEASCIRTREL 237
Cdd:PTZ00431 232 GLYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-236 |
2.78e-28 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 104.40 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 164 EDLIDAVTGLSGSGPAY-------------------------------GAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 212
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYvflfiealadagvamglpreearelaaqtvlGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 533112486 213 VLESGGFRSLLINAVEASCIRTRE 236
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
4-98 |
1.22e-19 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 81.51 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 4 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDLATVSAlRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76
|
90
....*....|....*..
gi 533112486 82 IgADIEDRHIVVSCAAG 98
Cdd:pfam03807 77 L-SDLLKGKIVISIAAG 92
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
1-217 |
3.75e-16 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 76.55 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680 1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAfrPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07680 81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITN---RALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 161 EVEEDLIDAVTGLSGSGPAY----------GAAKM---------------------LLHSEQH-PGQLKDNVSSPGGATI 208
Cdd:PRK07680 156 VIEEDITRVSSDIVSCGPAFfsyllqrfidAAVEEtniskeeattlasemligmgkLLEKGLYtLPTLQEKVCVKGGITG 235
|
....*....
gi 533112486 209 HALHVLESG 217
Cdd:PRK07680 236 EGIKVLEEE 244
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
3-183 |
2.98e-10 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 59.40 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 3 VGFIGAGQLAFALAKGFTAAGVLAAHKIM--ASSPDMDLATVSAlRKMGVKLTPHNKETVQHSDVLFLAVKP-HIIPFIL 79
Cdd:PRK06928 4 IGFIGYGSMADMIATKLLETEVATPEEIIlySSSKNEHFNQLYD-KYPTVELADNEAEIFTKCDHSFICVPPlAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 80 DEIGADIEDRHiVVSCAAGVTISSIeKKLSAFRPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:PRK06928 83 DCAPVLTPDRH-VVSIAAGVSLDDL-LEITPGLQVSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157
|
170 180
....*....|....*....|....
gi 533112486 160 TEVEEDLIDAVTGLSGSGPAYGAA 183
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAA 181
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
1-176 |
5.10e-08 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 52.71 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK06476 1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 81 EIGADieDRHIVVSCAAGVTISSIEKklsAFRPAPRVIRCMTNTPVVVREGAT-VYAtgTHAQVEDgrLMEQLLSSVGFC 159
Cdd:PRK06476 80 ALRFR--PGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150
|
170
....*....|....*..
gi 533112486 160 TEVEEDLIDAVTGLSGS 176
Cdd:PRK06476 151 SEEEYDLLAAASALMAT 167
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
3-96 |
9.42e-07 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 48.24 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 3 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75
|
90
....*....|....*
gi 533112486 82 IGADIEDRhIVVSCA 96
Cdd:COG2085 76 LGDALAGK-IVIDAT 89
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-110 |
1.05e-04 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 42.88 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533112486 1 MSVGFIGAGQLAFALAKGFTAAG--VLAAHkimASSPDmdlATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 78
Cdd:COG5495 4 MKIGIIGAGRVGTALAAALRAAGheVVGVY---SRSPA---SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEV 77
|
90 100 110
....*....|....*....|....*....|....*
gi 533112486 79 LDEI---GADIEDrHIVVSCAAGVTISSIEKKLSA 110
Cdd:COG5495 78 AAGLaaaGALRPG-QLVVHTSGALGSDVLAPAARA 111
|
|
|